1ge8

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(New page: 200px<br /><applet load="1ge8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ge8, resolution 2.10&Aring;" /> '''PROLIFERATING CELL N...)
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'''PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) HOMOLOG FROM PYROCOCCUS FURIOSUS'''<br />
'''PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) HOMOLOG FROM PYROCOCCUS FURIOSUS'''<br />
==Overview==
==Overview==
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The proliferating cell nuclear antigen (PCNA) is now recognized as one of, the key proteins in DNA metabolic events because of its direct, interactions with many proteins involved in important cellular processes., We have determined the crystal structure of PCNA from a hyperthermophilic, archaeon, Pyrococcus furiosus (pfuPCNA), at 2.1 A resolution. pfuPCNA, forms a toroidal, ring-shaped structure consisting of homotrimeric, molecules, which is also observed in the PCNA crystals from human and, yeast. The overall structure of pfuPCNA is highly conserved with other, PCNA proteins, as well as with the bacterial ss clamp and the, bacteriophage gp45. This result shows that the three-dimensional structure, of the sliding clamp is conserved in the three domains of life. pfuPCNA, has two remarkable features compared with the human and yeast PCNA, molecules: it has more ion pairs and fewer intermolecular main chain, hydrogen bonds. The former may contribute to the thermal stability of, pfuPCNA, and the latter may be the cause of the stimulatory effect of, pfuPCNA on the DNA synthesizing activity of P. furiosus DNA polymerases in, the absence of the clamp loader replication factor C in vitro.
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The proliferating cell nuclear antigen (PCNA) is now recognized as one of the key proteins in DNA metabolic events because of its direct interactions with many proteins involved in important cellular processes. We have determined the crystal structure of PCNA from a hyperthermophilic archaeon, Pyrococcus furiosus (pfuPCNA), at 2.1 A resolution. pfuPCNA forms a toroidal, ring-shaped structure consisting of homotrimeric molecules, which is also observed in the PCNA crystals from human and yeast. The overall structure of pfuPCNA is highly conserved with other PCNA proteins, as well as with the bacterial ss clamp and the bacteriophage gp45. This result shows that the three-dimensional structure of the sliding clamp is conserved in the three domains of life. pfuPCNA has two remarkable features compared with the human and yeast PCNA molecules: it has more ion pairs and fewer intermolecular main chain hydrogen bonds. The former may contribute to the thermal stability of pfuPCNA, and the latter may be the cause of the stimulatory effect of pfuPCNA on the DNA synthesizing activity of P. furiosus DNA polymerases in the absence of the clamp loader replication factor C in vitro.
==About this Structure==
==About this Structure==
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1GE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GE8 OCA].
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1GE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GE8 OCA].
==Reference==
==Reference==
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[[Category: sliding clamp]]
[[Category: sliding clamp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:58:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:09 2008''

Revision as of 10:49, 21 February 2008

Image:1ge8.gif

1ge8, resolution 2.10Å

Drag the structure with the mouse to rotate

PROLIFERATING CELL NUCLEAR ANTIGEN (PCNA) HOMOLOG FROM PYROCOCCUS FURIOSUS

Overview

The proliferating cell nuclear antigen (PCNA) is now recognized as one of the key proteins in DNA metabolic events because of its direct interactions with many proteins involved in important cellular processes. We have determined the crystal structure of PCNA from a hyperthermophilic archaeon, Pyrococcus furiosus (pfuPCNA), at 2.1 A resolution. pfuPCNA forms a toroidal, ring-shaped structure consisting of homotrimeric molecules, which is also observed in the PCNA crystals from human and yeast. The overall structure of pfuPCNA is highly conserved with other PCNA proteins, as well as with the bacterial ss clamp and the bacteriophage gp45. This result shows that the three-dimensional structure of the sliding clamp is conserved in the three domains of life. pfuPCNA has two remarkable features compared with the human and yeast PCNA molecules: it has more ion pairs and fewer intermolecular main chain hydrogen bonds. The former may contribute to the thermal stability of pfuPCNA, and the latter may be the cause of the stimulatory effect of pfuPCNA on the DNA synthesizing activity of P. furiosus DNA polymerases in the absence of the clamp loader replication factor C in vitro.

About this Structure

1GE8 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Crystal structure of an archaeal DNA sliding clamp: proliferating cell nuclear antigen from Pyrococcus furiosus., Matsumiya S, Ishino Y, Morikawa K, Protein Sci. 2001 Jan;10(1):17-23. PMID:11266590

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